spacer Structure of neuronal nitric oxide synthase heme domain in complex with (R)-1,2-bis((2-amino-4-methylpyridin-6-yl)-methoxy)-propan-3-amine
Accession P29476search
Keywords Heme, FAD, Iron, 3D-structure, Complete proteome, FMN, Metal-binding, Cell projection, Ubl conjugation, Flavoprotein, Cell membrane, Alternative splicing, Membrane, Oxidoreductase, Direct protein sequencing, Reference proteome, Calmodulin-binding, NADP
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Polymers A B
Enzyme nomenclature
EC number ExPASy BRENDA search
Polymers A, B
Name nitric-oxide synthase, nitric-oxide synthase (NADPH dependent)
Comment The enzyme in brain, but not that induced in lung or liver by endotoxin, requires Ca2+. The stoichiometry is not clear, but may involve a two-electron and a one-electron oxidation step.
Binds FAD, FMN, heme (iron protoporphyrin IX) and tetrahydrobiopterin. This eukaryotic enzyme, which is found in plants and animals [1-3], consists of oxygenase and reductase domains that are linked via a regulatory calmodulin-binding domain. Upon calcium-induced calmodulin binding, the reductase and oxygenase domains form a complex, allowing electrons to flow from NADPH via FAD and FMN to the active center. May produce superoxide under certain conditions. cf. EC, nitric-oxide synthase [NAD(P)H dependent].